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利福布汀与人血清白蛋白相互作用的光谱研究
引用本文:王丛霞,叶玲,闫芳菲,王楠,余沛霖.利福布汀与人血清白蛋白相互作用的光谱研究[J].高等学校化学学报,2007,28(12):2280-2283.
作者姓名:王丛霞  叶玲  闫芳菲  王楠  余沛霖
作者单位:首都医科大学化学生物学与药学院,北京,100069
摘    要:用荧光光谱法和圆二色谱法研究了利福布汀(RB)与人血清白蛋白(HSA)的相互作用. 结果表明, RB与HSA之间的相互作用主要是疏水作用, 作用机制是静态猝灭与动态猝灭的结合. 其结合常数(Ka)在106数量级, 说明RB和HSA有很强的结合. 此外, 探讨了金属离子(Cu2+, Zn2+, Mg2+ 和Ca2+)对RB与HSA结合常数的影响. 同步荧光光谱和圆二色谱数据表明, RB可导致HSA的构象改变.

关 键 词:利福布汀  人血清白蛋白  荧光猝灭  圆二色谱
文章编号:0251-0790(2007)12-2280-04
收稿时间:2007-03-29
修稿时间:2007年3月29日

Spectroscopic Studies on the Interaction Between Rifabutin and Human Serum Albumin
WANG Cong-Xia,YE Ling,YAN Fang-Fei,WANG Nan,YU Pei-Lin.Spectroscopic Studies on the Interaction Between Rifabutin and Human Serum Albumin[J].Chemical Research In Chinese Universities,2007,28(12):2280-2283.
Authors:WANG Cong-Xia  YE Ling  YAN Fang-Fei  WANG Nan  YU Pei-Lin
Institution:School of Chemical Biology and Pharmaceutical Sciences, Capital University of Medical Sciences, Beijing 100069, China
Abstract:The binding mechanism between Rifabutin(RB) and human serum albumin(HSA) was studied by fluorescence spectroscopy and CD.The results show that RB quenched the intrinsic fluorescence of HSA via a combination of static and dynamic quenching processes and hydrophobic interaction played a major role in stabilizing the RB-HSA complex.The binding constant Ka was calculated to be in the order of 106,indicating a strong interaction between RB and HSA.In addition,influences of metal ion(Cu2 ,Zn2 ,Mg2 and Ca2 ) on Ka were studied.Moreover,synchronous fluorescence spectroscopy and circular dichroism(CD)reveal the conformational change of HSA upon binding with RB.
Keywords:Rifabutin(RB)  Human serum albumin(HSA)  Fluorescence spectroscopy  Circular dichroism
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